Evidence map›Paper›PMID 20622019›Full record

ArticleThe Journal of biological chemistry2010

Initiation by a eukaryotic RNA-dependent RNA polymerase requires looping of the template end and is influenced by the template-tailing activity of an associated uridyltransferase.

Kristin Benjamin Talsky, Kathleen Collins

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.4field-weighted citation impact, top 38% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

13 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Multigenerational Regulation of theAnnual review of genetics · 2019
    Review
  5. Transgenerational function ofRNA (New York, N.Y.) · 2017
    Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Kristin Benjamin TalskyDepartment of Molecular and Cell Biology, University of California, Berkeley, California 94720, USA.
Kathleen Collins
University of California, Berkeley · US

Funding

STRUCTURE AND FUNCTION OF TELOMERASER01GM054198 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI COLLINS, KATHLEEN · 1996 to 2018
$5.4M
NIGMS NIH HHS GM54198NIGMS NIH HHS R01 GM054198
6 · The paper itself

Abstract

A conserved family of eukaryotic RNA-dependent RNA polymerases (RDRs) initiates or amplifies the production of small RNAs to provide sequence specificity for gene regulation by Argonaute/Piwi proteins. RDR-dependent silencing processes affect the genotype-phenotype relationship in many eukaryotes, but the principles that underlie the specificity of RDR template selection and product synthesis are largely unknown. Here, we characterize the initiation specificity of the Tetrahymena RDR, Rdr1, as a heterologously expressed single subunit and in the context of its biologically assembled multisubunit complexes (RDRCs). Truncation analysis of recombinant Rdr1 revealed domain requirements different from those of the only other similarly characterized RDR, suggesting that there are subfamilies of the RDR enzyme with distinct structural requirements for activity. We demonstrate an apparently obligate Rdr1 mechanism of initiation in which the template end is looped to provide the hydroxyl group priming the synthesis of dsRNA. RDRC subunits with poly(U) polymerase activity can act on the template end prior to looping to increase the duplex length of product, thus impacting the small RNA sequences generated by the RDRC-coupled Dicer. Overall, our findings give new perspective on mechanisms of RDR initiation and demonstrate that non-RDR subunits of an RDRC can affect the specificity of product synthesis.

Indexed as

Base SequenceDNA ReplicationFungal ProteinsGene SilencingMolecular Sequence DataNucleotidyltransferasesPhosphatesProtein Structure, TertiaryProtein SubunitsRibonuclease IIIRibonucleotidesRNA-Dependent RNA PolymeraseRNA, Double-StrandedRNA, UntranslatedSubstrate SpecificityTetrahymenaFungal ProteinsNucleotidyltransferasesPhosphatespoly U polymeraseProtein SubunitsQDE1 protein, Neurospora crassaRibonuclease IIIRibonucleotidesRNA-Dependent RNA PolymeraseRNA, Double-StrandedRNA, UntranslatedUridine

Identifiers

PMID20622019
PMCPMC2934629
OpenAlexW2019858400

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.